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@article{1353957,
author = {Lattová, Erika and Bryant, Joseph and Skřičková, Jana and Zdráhal, Zbyněk and Popovič, Mikuláš},
article_location = {Washington},
article_number = {8},
doi = {http://dx.doi.org/10.1021/acs.jproteome.6b00346},
keywords = {Biopsy; cancer cells; EndoH; glycans; glycosylation; mass spectrometry; tumor tissue},
language = {eng},
issn = {1535-3893},
journal = {JOURNAL OF PROTEOME RESEARCH},
title = {Efficient Procedure for N-Glycan Analyses and Detection of Endo H-Like Activity in Human Tumor Specimens},
url = {http://pubs.acs.org/doi/abs/10.1021/acs.jproteome.6b00346},
volume = {15},
year = {2016}
}
TY - JOUR
ID - 1353957
AU - Lattová, Erika - Bryant, Joseph - Skřičková, Jana - Zdráhal, Zbyněk - Popovič, Mikuláš
PY - 2016
TI - Efficient Procedure for N-Glycan Analyses and Detection of Endo H-Like Activity in Human Tumor Specimens
JF - JOURNAL OF PROTEOME RESEARCH
VL - 15
IS - 8
SP - 2777-2786
EP - 2777-2786
PB - AMER CHEMICAL SOC
SN - 15353893
KW - Biopsy
KW - cancer cells
KW - EndoH
KW - glycans
KW - glycosylation
KW - mass spectrometry
KW - tumor tissue
UR - http://pubs.acs.org/doi/abs/10.1021/acs.jproteome.6b00346
L2 - http://pubs.acs.org/doi/abs/10.1021/acs.jproteome.6b00346
N2 - Although the importance of glycosylation has been thoroughly recognized in association with a number of biological processes, efficient assessments of glycans have been hampered by both the limited size of specimens and lengthy sample preparations, particularly in clinical settings. Here we report a simple preparative method for N-glycan analyses. It involves only short one-step chloroform methanol extraction in presence or absence of water prior to PNGase F deglycosylation. The procedure was successfully applied to the investigation of N-glycans obtained from small numbers of in vitro cultured cancer cells (<= 1 x 10(5)) and to tumor tissues, including patient biopsies of small size. MALDI-MS analysis confirmed the efficient release of all N-glycan types including complex forms with poly-N-acetyllactosamine chains. In addition, nonaqueous extraction of specimens from several established cancer cell lines, as well as patient tumor tissues, yielded high-mannose glycans with one G1cNAc moiety (Man(3-9)GlcNAc), strongly suggesting preservation of enzymatic activity analogous to Endo H enzyme. In summary, the method is both a step toward the practical use of glycan profiling and a way to detect Endo H-like activity in cancer specimens.
ER -
LATTOVÁ, Erika, Joseph BRYANT, Jana SKŘIČKOVÁ, Zbyněk ZDRÁHAL a Mikuláš POPOVIČ. Efficient Procedure for N-Glycan Analyses and Detection of Endo H-Like Activity in Human Tumor Specimens. \textit{JOURNAL OF PROTEOME RESEARCH}. Washington: AMER CHEMICAL SOC, 2016, roč.~15, č.~8, s.~2777-2786. ISSN~1535-3893. Dostupné z: https://dx.doi.org/10.1021/acs.jproteome.6b00346.
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